Crystals of ferric ion-binding-protein have been grown and a complete data collection has been done to 1.6 E resolution. This first crystal structure of the iron-transporter ferric ion-binding protein from hFBP reveals the structural basis for iron uptake and transport required by several important bacterial pathogens. We seek to collect synchrotron data from hFBP crystals and to get a better resolution than 1.6 E using the SR source. A high-resolution structure of the Fe3+ center is essential to study the very interesting geometry around the iron center with precision. With a higher resolution (<1.3 E) we can refine anisotropic thermal parameters and add riding hydrogens. Preliminary results on other systems has shown that we can get Fe-ligand distance errors of <0.01 E using SHELX. Two different mutants of the hFBP protein have been obtained, hFBP-Y195A and hFBP-H9A. Crystals have been grown from these mutants and are smaller than the native crystals.